메뉴 건너뛰기




Volumn 1819, Issue 6, 2012, Pages 521-530

Ubiquitin and assembly of export competent mRNP

Author keywords

MRNA export; MRNP assembly; Nuclear pore complex; Quality control; Transcription; Ubiquitin

Indexed keywords

HISTONE H2B; MESSENGER RNA; NUCLEOPROTEIN; RIBONUCLEOPROTEIN; RNA POLYMERASE II; UBIQUITIN;

EID: 84860481614     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2011.12.006     Document Type: Review
Times cited : (17)

References (127)
  • 1
    • 42449084129 scopus 로고    scopus 로고
    • Protein factors in pre-mRNA 3'-end processing
    • Mandel C.R., Bai Y., Tong L. Protein factors in pre-mRNA 3'-end processing. Cell. Mol. Life Sci. 2008, 65:1099-1122.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1099-1122
    • Mandel, C.R.1    Bai, Y.2    Tong, L.3
  • 3
    • 70449641057 scopus 로고    scopus 로고
    • Progression through the RNA polymerase II CTD cycle
    • Buratowski S. Progression through the RNA polymerase II CTD cycle. Mol. Cell 2009, 36:541-546.
    • (2009) Mol. Cell , vol.36 , pp. 541-546
    • Buratowski, S.1
  • 4
    • 0037154964 scopus 로고    scopus 로고
    • A conserved mRNA export machinery coupled to pre-mRNA splicing
    • Reed R., Hurt E. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell 2002, 108:523-531.
    • (2002) Cell , vol.108 , pp. 523-531
    • Reed, R.1    Hurt, E.2
  • 5
    • 0141469976 scopus 로고    scopus 로고
    • Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export
    • Strasser K., Hurt E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 2000, 19:410-420.
    • (2000) EMBO J. , vol.19 , pp. 410-420
    • Strasser, K.1    Hurt, E.2
  • 7
    • 0037175374 scopus 로고    scopus 로고
    • REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
    • Gatfield D., Izaurralde E. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J. Cell Biol. 2002, 159:579-588.
    • (2002) J. Cell Biol. , vol.159 , pp. 579-588
    • Gatfield, D.1    Izaurralde, E.2
  • 8
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang Y., Gattoni R., Stevenin J., Steitz J.A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 2003, 11:837-843.
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 9
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang Y., Steitz J.A. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol. Cell 2001, 7:899-905.
    • (2001) Mol. Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 10
    • 0842288796 scopus 로고    scopus 로고
    • The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA
    • Gilbert W., Guthrie C. The Glc7p nuclear phosphatase promotes mRNA export by facilitating association of Mex67p with mRNA. Mol. Cell 2004, 13:201-212.
    • (2004) Mol. Cell , vol.13 , pp. 201-212
    • Gilbert, W.1    Guthrie, C.2
  • 11
    • 0037040895 scopus 로고    scopus 로고
    • Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p
    • Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. J. Biol. Chem. 2002, 277:7752-7760.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7752-7760
    • Green, D.M.1    Marfatia, K.A.2    Crafton, E.B.3    Zhang, X.4    Cheng, X.5    Corbett, A.H.6
  • 16
    • 71749088820 scopus 로고    scopus 로고
    • Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure
    • Batisse J., Batisse C., Budd A., Bottcher B., Hurt E. Purification of nuclear poly(A)-binding protein Nab2 reveals association with the yeast transcriptome and a messenger ribonucleoprotein core structure. J. Biol. Chem. 2009, 284:34911-34917.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34911-34917
    • Batisse, J.1    Batisse, C.2    Budd, A.3    Bottcher, B.4    Hurt, E.5
  • 17
    • 27944474017 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim
    • Lund M.K., Guthrie C. The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim. Mol. Cell 2005, 20:645-651.
    • (2005) Mol. Cell , vol.20 , pp. 645-651
    • Lund, M.K.1    Guthrie, C.2
  • 19
    • 4043129097 scopus 로고    scopus 로고
    • Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors
    • Yu M.C., Bachand F., McBride A.E., Komili S., Casolari J.M., Silver P.A. Arginine methyltransferase affects interactions and recruitment of mRNA processing and export factors. Genes Dev. 2004, 18:2024-2035.
    • (2004) Genes Dev. , vol.18 , pp. 2024-2035
    • Yu, M.C.1    Bachand, F.2    McBride, A.E.3    Komili, S.4    Casolari, J.M.5    Silver, P.A.6
  • 20
    • 21844435714 scopus 로고    scopus 로고
    • Npl3 is an antagonist of mRNA 3' end formation by RNA polymerase II
    • Bucheli M.E., Buratowski S. Npl3 is an antagonist of mRNA 3' end formation by RNA polymerase II. EMBO J. 2005, 24:2150-2160.
    • (2005) EMBO J. , vol.24 , pp. 2150-2160
    • Bucheli, M.E.1    Buratowski, S.2
  • 22
    • 0034329461 scopus 로고    scopus 로고
    • A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae
    • Chavez S., Beilharz T., Rondon A.G., Erdjument-Bromage H., Tempst P., Svejstrup J.Q., Lithgow T., Aguilera A. A protein complex containing Tho2, Hpr1, Mft1 and a novel protein, Thp2, connects transcription elongation with mitotic recombination in Saccharomyces cerevisiae. EMBO J. 2000, 19:5824-5834.
    • (2000) EMBO J. , vol.19 , pp. 5824-5834
    • Chavez, S.1    Beilharz, T.2    Rondon, A.G.3    Erdjument-Bromage, H.4    Tempst, P.5    Svejstrup, J.Q.6    Lithgow, T.7    Aguilera, A.8
  • 23
    • 0036889334 scopus 로고    scopus 로고
    • Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p
    • Zenklusen D., Vinciguerra P., Wyss J.C., Stutz F. Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol. Cell. Biol. 2002, 22:8241-8253.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8241-8253
    • Zenklusen, D.1    Vinciguerra, P.2    Wyss, J.C.3    Stutz, F.4
  • 24
    • 0036645687 scopus 로고    scopus 로고
    • The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability
    • Jimeno S., Rondon A.G., Luna R., Aguilera A. The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J. 2002, 21:3526-3535.
    • (2002) EMBO J. , vol.21 , pp. 3526-3535
    • Jimeno, S.1    Rondon, A.G.2    Luna, R.3    Aguilera, A.4
  • 26
    • 58649121693 scopus 로고    scopus 로고
    • Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3' end processing factor Pcf11
    • Johnson S.A., Cubberley G., Bentley D.L. Cotranscriptional recruitment of the mRNA export factor Yra1 by direct interaction with the 3' end processing factor Pcf11. Mol. Cell 2009, 33:215-226.
    • (2009) Mol. Cell , vol.33 , pp. 215-226
    • Johnson, S.A.1    Cubberley, G.2    Bentley, D.L.3
  • 30
    • 70349306459 scopus 로고    scopus 로고
    • Assembly of an export-competent mRNP is needed for efficient release of the 3'-end processing complex after polyadenylation
    • Qu X., Lykke-Andersen S., Nasser T., Saguez C., Bertrand E., Jensen T.H., Moore C. Assembly of an export-competent mRNP is needed for efficient release of the 3'-end processing complex after polyadenylation. Mol. Cell. Biol. 2009, 29:5327-5338.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5327-5338
    • Qu, X.1    Lykke-Andersen, S.2    Nasser, T.3    Saguez, C.4    Bertrand, E.5    Jensen, T.H.6    Moore, C.7
  • 31
    • 0141819093 scopus 로고    scopus 로고
    • Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
    • Huertas P., Aguilera A. Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol. Cell 2003, 12:711-721.
    • (2003) Mol. Cell , vol.12 , pp. 711-721
    • Huertas, P.1    Aguilera, A.2
  • 34
    • 79956097915 scopus 로고    scopus 로고
    • Linking gene regulation to mRNA production and export
    • Rodriguez-Navarro S., Hurt E. Linking gene regulation to mRNA production and export. Curr. Opin. Cell Biol. 2011, 23:1-8.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 1-8
    • Rodriguez-Navarro, S.1    Hurt, E.2
  • 35
    • 77955664901 scopus 로고    scopus 로고
    • The interface between transcription and mRNP export: from THO to THSC/TREX-2
    • Rondon A.G., Jimeno S., Aguilera A. The interface between transcription and mRNP export: from THO to THSC/TREX-2. Biochim. Biophys. Acta 2010, 1799:533-538.
    • (2010) Biochim. Biophys. Acta , vol.1799 , pp. 533-538
    • Rondon, A.G.1    Jimeno, S.2    Aguilera, A.3
  • 37
    • 77953589098 scopus 로고    scopus 로고
    • Connecting the transcription site to the nuclear pore: a multi-tether process that regulates gene expression
    • Dieppois G., Stutz F. Connecting the transcription site to the nuclear pore: a multi-tether process that regulates gene expression. J. Cell Sci. 2010, 123:1989-1999.
    • (2010) J. Cell Sci. , vol.123 , pp. 1989-1999
    • Dieppois, G.1    Stutz, F.2
  • 39
    • 57349185689 scopus 로고    scopus 로고
    • The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability
    • Gonzalez-Aguilera C., Tous C., Gomez-Gonzalez B., Huertas P., Luna R., Aguilera A. The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Mol. Biol. Cell 2008, 19:4310-4318.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4310-4318
    • Gonzalez-Aguilera, C.1    Tous, C.2    Gomez-Gonzalez, B.3    Huertas, P.4    Luna, R.5    Aguilera, A.6
  • 40
    • 77957370148 scopus 로고    scopus 로고
    • In vivo imaging of labelled endogenous beta-actin mRNA during nucleocytoplasmic transport
    • Grunwald D., Singer R.H. In vivo imaging of labelled endogenous beta-actin mRNA during nucleocytoplasmic transport. Nature 2010, 467:604-607.
    • (2010) Nature , vol.467 , pp. 604-607
    • Grunwald, D.1    Singer, R.H.2
  • 41
  • 42
    • 79957496447 scopus 로고    scopus 로고
    • Keeping mRNPs in check during assembly and export through nuclear pores
    • Tutucci E., Stutz F. Keeping mRNPs in check during assembly and export through nuclear pores. Nat. Rev. Mol. Cell Biol. 2011, 12(6):377-384.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , Issue.6 , pp. 377-384
    • Tutucci, E.1    Stutz, F.2
  • 43
    • 0742304306 scopus 로고    scopus 로고
    • Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1
    • Galy V., Gadal O., Fromont-Racine M., Romano A., Jacquier A., Nehrbass U. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell 2004, 116:63-73.
    • (2004) Cell , vol.116 , pp. 63-73
    • Galy, V.1    Gadal, O.2    Fromont-Racine, M.3    Romano, A.4    Jacquier, A.5    Nehrbass, U.6
  • 44
    • 15444368318 scopus 로고    scopus 로고
    • Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export
    • Vinciguerra P., Iglesias N., Camblong J., Zenklusen D., Stutz F. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J. 2005, 24:813-823.
    • (2005) EMBO J. , vol.24 , pp. 813-823
    • Vinciguerra, P.1    Iglesias, N.2    Camblong, J.3    Zenklusen, D.4    Stutz, F.5
  • 45
    • 0037884974 scopus 로고    scopus 로고
    • An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components
    • Estruch F., Cole C.N. An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components. Mol. Biol. Cell 2003, 14:1664-1676.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1664-1676
    • Estruch, F.1    Cole, C.N.2
  • 46
    • 0032080030 scopus 로고    scopus 로고
    • Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export
    • Snay-Hodge C.A., Colot H.V., Goldstein A.L., Cole C.N. Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein essential for RNA export. EMBO J. 1998, 17:2663-2676.
    • (1998) EMBO J. , vol.17 , pp. 2663-2676
    • Snay-Hodge, C.A.1    Colot, H.V.2    Goldstein, A.L.3    Cole, C.N.4
  • 47
    • 0033569962 scopus 로고    scopus 로고
    • Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells
    • Hodge C.A., Colot H.V., Stafford P., Cole C.N. Rat8p/Dbp5p is a shuttling transport factor that interacts with Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 cells. EMBO J. 1999, 18:5778-5788.
    • (1999) EMBO J. , vol.18 , pp. 5778-5788
    • Hodge, C.A.1    Colot, H.V.2    Stafford, P.3    Cole, C.N.4
  • 48
    • 0033569797 scopus 로고    scopus 로고
    • The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p
    • Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., Stutz F. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J. 1999, 18:5761-5777.
    • (1999) EMBO J. , vol.18 , pp. 5761-5777
    • Strahm, Y.1    Fahrenkrog, B.2    Zenklusen, D.3    Rychner, E.4    Kantor, J.5    Rosbach, M.6    Stutz, F.7
  • 49
    • 33745736445 scopus 로고    scopus 로고
    • Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export
    • Alcazar-Roman A.R., Tran E.J., Guo S., Wente S.R. Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5 for nuclear mRNA export. Nat. Cell Biol. 2006, 8:711-716.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 711-716
    • Alcazar-Roman, A.R.1    Tran, E.J.2    Guo, S.3    Wente, S.R.4
  • 50
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export
    • Weirich C.S., Erzberger J.P., Flick J.S., Berger J.M., Thorner J., Weis K. Activation of the DExD/H-box protein Dbp5 by the nuclear-pore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat. Cell Biol. 2006, 8:668-676.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 668-676
    • Weirich, C.S.1    Erzberger, J.P.2    Flick, J.S.3    Berger, J.M.4    Thorner, J.5    Weis, K.6
  • 51
    • 44449169243 scopus 로고    scopus 로고
    • Regulation of mRNP dynamics along the export pathway
    • Iglesias N., Stutz F. Regulation of mRNP dynamics along the export pathway. FEBS Lett. 2008, 582:1987-1996.
    • (2008) FEBS Lett. , vol.582 , pp. 1987-1996
    • Iglesias, N.1    Stutz, F.2
  • 52
    • 36749016233 scopus 로고    scopus 로고
    • The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events
    • Tran E.J., Zhou Y., Corbett A.H., Wente S.R. The DEAD-box protein Dbp5 controls mRNA export by triggering specific RNA:protein remodeling events. Mol. Cell 2007, 28:850-859.
    • (2007) Mol. Cell , vol.28 , pp. 850-859
    • Tran, E.J.1    Zhou, Y.2    Corbett, A.H.3    Wente, S.R.4
  • 53
  • 54
    • 79954598438 scopus 로고    scopus 로고
    • A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP(6) in mRNA export
    • Montpetit B., Thomsen N.D., Helmke K.J., Seeliger M.A., Berger J.M., Weis K. A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP(6) in mRNA export. Nature 2011, 472:238-242.
    • (2011) Nature , vol.472 , pp. 238-242
    • Montpetit, B.1    Thomsen, N.D.2    Helmke, K.J.3    Seeliger, M.A.4    Berger, J.M.5    Weis, K.6
  • 55
    • 79956300418 scopus 로고    scopus 로고
    • The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1
    • Noble K.N., Tran E.J., Alcazar-Roman A.R., Hodge C.A., Cole C.N., Wente S.R. The Dbp5 cycle at the nuclear pore complex during mRNA export II: nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1. Genes Dev. 2011, 25:1065-1077.
    • (2011) Genes Dev. , vol.25 , pp. 1065-1077
    • Noble, K.N.1    Tran, E.J.2    Alcazar-Roman, A.R.3    Hodge, C.A.4    Cole, C.N.5    Wente, S.R.6
  • 57
    • 0030969145 scopus 로고    scopus 로고
    • Isolation and molecular characterization of mRNA transport mutants in Schizosaccharomyces pombe
    • Azad A.K., Tani T., Shiki N., Tsuneyoshi S., Urushiyama S., Ohshima Y. Isolation and molecular characterization of mRNA transport mutants in Schizosaccharomyces pombe. Mol. Biol. Cell 1997, 8:825-841.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 825-841
    • Azad, A.K.1    Tani, T.2    Shiki, N.3    Tsuneyoshi, S.4    Urushiyama, S.5    Ohshima, Y.6
  • 58
    • 0034659266 scopus 로고    scopus 로고
    • A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport
    • Duncan K., Umen J.G., Guthrie C. A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr. Biol. 2000, 10:687-696.
    • (2000) Curr. Biol. , vol.10 , pp. 687-696
    • Duncan, K.1    Umen, J.G.2    Guthrie, C.3
  • 59
  • 60
    • 0042812051 scopus 로고    scopus 로고
    • The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae
    • Rodriguez M.S., Gwizdek C., Haguenauer-Tsapis R., Dargemont C. The HECT ubiquitin ligase Rsp5p is required for proper nuclear export of mRNA in Saccharomyces cerevisiae. Traffic 2003, 4:566-575.
    • (2003) Traffic , vol.4 , pp. 566-575
    • Rodriguez, M.S.1    Gwizdek, C.2    Haguenauer-Tsapis, R.3    Dargemont, C.4
  • 64
    • 65249166493 scopus 로고    scopus 로고
    • Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins
    • Grabbe C., Dikic I. Functional roles of ubiquitin-like domain (ULD) and ubiquitin-binding domain (UBD) containing proteins. Chem. Rev. 2009, 109:1481-1494.
    • (2009) Chem. Rev. , vol.109 , pp. 1481-1494
    • Grabbe, C.1    Dikic, I.2
  • 65
    • 33646064427 scopus 로고    scopus 로고
    • Structural complexity in ubiquitin recognition
    • Harper J.W., Schulman B.A. Structural complexity in ubiquitin recognition. Cell 2006, 124:1133-1136.
    • (2006) Cell , vol.124 , pp. 1133-1136
    • Harper, J.W.1    Schulman, B.A.2
  • 67
    • 0036215896 scopus 로고    scopus 로고
    • Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1
    • Grant R.P., Hurt E., Neuhaus D., Stewart M. Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1. Nat. Struct. Biol. 2002, 9:247-251.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 247-251
    • Grant, R.P.1    Hurt, E.2    Neuhaus, D.3    Stewart, M.4
  • 68
    • 0037459067 scopus 로고    scopus 로고
    • Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution
    • Grant R.P., Neuhaus D., Stewart M. Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution. J. Mol. Biol. 2003, 326:849-858.
    • (2003) J. Mol. Biol. , vol.326 , pp. 849-858
    • Grant, R.P.1    Neuhaus, D.2    Stewart, M.3
  • 70
    • 67650543863 scopus 로고    scopus 로고
    • Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats
    • Hobeika M., Brockmann C., Gruessing F., Neuhaus D., Divita G., Stewart M., Dargemont C. Structural requirements for the ubiquitin-associated domain of the mRNA export factor Mex67 to bind its specific targets, the transcription elongation THO complex component Hpr1 and nucleoporin FXFG repeats. J. Biol. Chem. 2009, 284:17575-17583.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17575-17583
    • Hobeika, M.1    Brockmann, C.2    Gruessing, F.3    Neuhaus, D.4    Divita, G.5    Stewart, M.6    Dargemont, C.7
  • 71
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: structure and function of the deubiquitinases
    • Komander D., Clague M.J., Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol. 2009, 10:550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 73
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 2002, 418:104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 74
    • 0037248593 scopus 로고    scopus 로고
    • A conserved RING finger protein required for histone H2B monoubiquitination and cell size control
    • Hwang W.W., Venkatasubrahmanyam S., Ianculescu A.G., Tong A., Boone C., Madhani H.D. A conserved RING finger protein required for histone H2B monoubiquitination and cell size control. Mol. Cell 2003, 11:261-266.
    • (2003) Mol. Cell , vol.11 , pp. 261-266
    • Hwang, W.W.1    Venkatasubrahmanyam, S.2    Ianculescu, A.G.3    Tong, A.4    Boone, C.5    Madhani, H.D.6
  • 75
    • 0034695456 scopus 로고    scopus 로고
    • Rad6-dependent ubiquitination of histone H2B in yeast
    • Robzyk K., Recht J., Osley M.A. Rad6-dependent ubiquitination of histone H2B in yeast. Science 2000, 287:501-504.
    • (2000) Science , vol.287 , pp. 501-504
    • Robzyk, K.1    Recht, J.2    Osley, M.A.3
  • 79
    • 40849106789 scopus 로고    scopus 로고
    • Histone ubiquitination: triggering gene activity
    • Weake V.M., Workman J.L. Histone ubiquitination: triggering gene activity. Mol. Cell 2008, 29:653-663.
    • (2008) Mol. Cell , vol.29 , pp. 653-663
    • Weake, V.M.1    Workman, J.L.2
  • 81
    • 44649179312 scopus 로고    scopus 로고
    • Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export
    • Kohler A., Schneider M., Cabal G.G., Nehrbass U., Hurt E. Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nat. Cell Biol. 2008, 10:707-715.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 707-715
    • Kohler, A.1    Schneider, M.2    Cabal, G.G.3    Nehrbass, U.4    Hurt, E.5
  • 82
    • 77952519938 scopus 로고    scopus 로고
    • Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module
    • Kohler A., Zimmerman E., Schneider M., Hurt E., Zheng N. Structural basis for assembly and activation of the heterotetrameric SAGA histone H2B deubiquitinase module. Cell 2010, 141:606-617.
    • (2010) Cell , vol.141 , pp. 606-617
    • Kohler, A.1    Zimmerman, E.2    Schneider, M.3    Hurt, E.4    Zheng, N.5
  • 85
    • 29144472375 scopus 로고    scopus 로고
    • A role for the CPF 3'-end processing machinery in RNAP II-dependent gene looping
    • Ansari A., Hampsey M. A role for the CPF 3'-end processing machinery in RNAP II-dependent gene looping. Genes Dev. 2005, 19:2969-2978.
    • (2005) Genes Dev. , vol.19 , pp. 2969-2978
    • Ansari, A.1    Hampsey, M.2
  • 87
    • 72749098124 scopus 로고    scopus 로고
    • Gene loops function to maintain transcriptional memory through interaction with the nuclear pore complex
    • Tan-Wong S.M., Wijayatilake H.D., Proudfoot N.J. Gene loops function to maintain transcriptional memory through interaction with the nuclear pore complex. Genes Dev. 2009, 23:2610-2624.
    • (2009) Genes Dev. , vol.23 , pp. 2610-2624
    • Tan-Wong, S.M.1    Wijayatilake, H.D.2    Proudfoot, N.J.3
  • 89
    • 79952122633 scopus 로고    scopus 로고
    • Dynamic histone acetylation is critical for cotranscriptional spliceosome assembly and spliceosomal rearrangements
    • Gunderson F.Q., Merkhofer E.C., Johnson T.L. Dynamic histone acetylation is critical for cotranscriptional spliceosome assembly and spliceosomal rearrangements. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:2004-2009.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2004-2009
    • Gunderson, F.Q.1    Merkhofer, E.C.2    Johnson, T.L.3
  • 90
    • 44149124228 scopus 로고    scopus 로고
    • Cracking the RNA polymerase II CTD code
    • Egloff S., Murphy S. Cracking the RNA polymerase II CTD code. Trends Genet. 2008, 24:280-288.
    • (2008) Trends Genet. , vol.24 , pp. 280-288
    • Egloff, S.1    Murphy, S.2
  • 92
    • 40349114502 scopus 로고    scopus 로고
    • The Rpb4 subunit of RNA polymerase II contributes to cotranscriptional recruitment of 3' processing factors
    • Runner V.M., Podolny V., Buratowski S. The Rpb4 subunit of RNA polymerase II contributes to cotranscriptional recruitment of 3' processing factors. Mol. Cell. Biol. 2008, 28:1883-1891.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1883-1891
    • Runner, V.M.1    Podolny, V.2    Buratowski, S.3
  • 93
    • 0038107498 scopus 로고    scopus 로고
    • Rpb4p, a subunit of RNA polymerase II, mediates mRNA export during stress
    • Farago M., Nahari T., Hammel C., Cole C.N., Choder M. Rpb4p, a subunit of RNA polymerase II, mediates mRNA export during stress. Mol. Biol. Cell 2003, 14:2744-2755.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2744-2755
    • Farago, M.1    Nahari, T.2    Hammel, C.3    Cole, C.N.4    Choder, M.5
  • 94
    • 78149478886 scopus 로고    scopus 로고
    • RNA polymerase II subunits link transcription and mRNA decay to translation
    • Harel-Sharvit L., Eldad N., Haimovich G., Barkai O., Duek L., Choder M. RNA polymerase II subunits link transcription and mRNA decay to translation. Cell 2010, 143:552-563.
    • (2010) Cell , vol.143 , pp. 552-563
    • Harel-Sharvit, L.1    Eldad, N.2    Haimovich, G.3    Barkai, O.4    Duek, L.5    Choder, M.6
  • 95
    • 79958061525 scopus 로고    scopus 로고
    • The Prp19 complex is a novel transcription elongation factor required for TREX occupancy at transcribed genes
    • Chanarat S., Seizl M., Strässer K. The Prp19 complex is a novel transcription elongation factor required for TREX occupancy at transcribed genes. Genes Dev. 2011, 25:1147-1158.
    • (2011) Genes Dev. , vol.25 , pp. 1147-1158
    • Chanarat, S.1    Seizl, M.2    Strässer, K.3
  • 97
    • 17644386183 scopus 로고    scopus 로고
    • The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing
    • Muratani M., Kung C., Shokat K.M., Tansey W.P. The F box protein Dsg1/Mdm30 is a transcriptional coactivator that stimulates Gal4 turnover and cotranscriptional mRNA processing. Cell 2005, 120:887-899.
    • (2005) Cell , vol.120 , pp. 887-899
    • Muratani, M.1    Kung, C.2    Shokat, K.M.3    Tansey, W.P.4
  • 98
    • 3343003673 scopus 로고    scopus 로고
    • Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes
    • Abruzzi K.C., Lacadie S., Rosbash M. Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes. EMBO J. 2004, 23:2620-2631.
    • (2004) EMBO J. , vol.23 , pp. 2620-2631
    • Abruzzi, K.C.1    Lacadie, S.2    Rosbash, M.3
  • 100
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J., Tollervey D. The many pathways of RNA degradation. Cell 2009, 136:763-776.
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 101
    • 51549111789 scopus 로고    scopus 로고
    • Quality control of mRNP in the nucleus
    • Schmid M., Jensen T.H. Quality control of mRNP in the nucleus. Chromosoma 2008, 117:419-429.
    • (2008) Chromosoma , vol.117 , pp. 419-429
    • Schmid, M.1    Jensen, T.H.2
  • 102
    • 0035807308 scopus 로고    scopus 로고
    • Quality control of mRNA 3'-end processing is linked to the nuclear exosome
    • Hilleren P., McCarthy T., Rosbash M., Parker R., Jensen T.H. Quality control of mRNA 3'-end processing is linked to the nuclear exosome. Nature 2001, 413:538-542.
    • (2001) Nature , vol.413 , pp. 538-542
    • Hilleren, P.1    McCarthy, T.2    Rosbash, M.3    Parker, R.4    Jensen, T.H.5
  • 103
    • 0036889142 scopus 로고    scopus 로고
    • Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation
    • Libri D., Dower K., Boulay J., Thomsen R., Rosbash M., Jensen T.H. Interactions between mRNA export commitment, 3'-end quality control, and nuclear degradation. Mol. Cell. Biol. 2002, 22:8254-8266.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8254-8266
    • Libri, D.1    Dower, K.2    Boulay, J.3    Thomsen, R.4    Rosbash, M.5    Jensen, T.H.6
  • 104
    • 27644511335 scopus 로고    scopus 로고
    • Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles
    • Palancade B., Zuccolo M., Loeillet S., Nicolas A., Doye V. Pml39, a novel protein of the nuclear periphery required for nuclear retention of improper messenger ribonucleoparticles. Mol. Biol. Cell 2005, 16:5258-5268.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5258-5268
    • Palancade, B.1    Zuccolo, M.2    Loeillet, S.3    Nicolas, A.4    Doye, V.5
  • 107
    • 0037417959 scopus 로고    scopus 로고
    • The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export
    • Green D.M., Johnson C.P., Hagan H., Corbett A.H. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:1010-1015.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1010-1015
    • Green, D.M.1    Johnson, C.P.2    Hagan, H.3    Corbett, A.H.4
  • 108
    • 58849125742 scopus 로고    scopus 로고
    • An endoribonuclease functionally linked to perinuclear mRNP quality control associates with the nuclear pore complexes
    • Skruzny M., Schneider C., Racz A., Weng J., Tollervey D., Hurt E. An endoribonuclease functionally linked to perinuclear mRNP quality control associates with the nuclear pore complexes. PLoS Biol. 2009, 7:e8.
    • (2009) PLoS Biol. , vol.7
    • Skruzny, M.1    Schneider, C.2    Racz, A.3    Weng, J.4    Tollervey, D.5    Hurt, E.6
  • 109
    • 41149157334 scopus 로고    scopus 로고
    • Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties?
    • Palancade B., Doye V. Sumoylating and desumoylating enzymes at nuclear pores: underpinning their unexpected duties?. Trends Cell Biol. 2008, 18:174-183.
    • (2008) Trends Cell Biol. , vol.18 , pp. 174-183
    • Palancade, B.1    Doye, V.2
  • 110
    • 9444259173 scopus 로고    scopus 로고
    • Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality
    • Zhao X., Wu C.Y., Blobel G. Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality. J. Cell Biol. 2004, 167:605-611.
    • (2004) J. Cell Biol. , vol.167 , pp. 605-611
    • Zhao, X.1    Wu, C.Y.2    Blobel, G.3
  • 111
    • 34548318654 scopus 로고    scopus 로고
    • A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance
    • Lewis A., Felberbaum R., Hochstrasser M. A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance. J. Cell Biol. 2007, 178:813-827.
    • (2007) J. Cell Biol. , vol.178 , pp. 813-827
    • Lewis, A.1    Felberbaum, R.2    Hochstrasser, M.3
  • 112
    • 13444310855 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of Yra1p in budding yeast
    • Kashyap A.K., Schieltz D., Yates J., Kellogg D.R. Biochemical and genetic characterization of Yra1p in budding yeast. Yeast 2005, 22:43-56.
    • (2005) Yeast , vol.22 , pp. 43-56
    • Kashyap, A.K.1    Schieltz, D.2    Yates, J.3    Kellogg, D.R.4
  • 114
  • 116
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel S.S., Belmont B.J., Sante J.M., Rexach M.F. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 2007, 129:83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 117
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K., Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 2001, 20:1320-1330.
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 119
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: nuclear pore complex structure, assembly, and function
    • Suntharalingam M., Wente S.R. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 2003, 4:775-789.
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 120
    • 34748839688 scopus 로고    scopus 로고
    • Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex
    • Terry L.J., Wente S.R. Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex. J. Cell Biol. 2007, 178:1121-1132.
    • (2007) J. Cell Biol. , vol.178 , pp. 1121-1132
    • Terry, L.J.1    Wente, S.R.2
  • 121
    • 0028607144 scopus 로고
    • A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution
    • Doye V., Wepf R., Hurt E.C. A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution. EMBO J. 1994, 13:6062-6075.
    • (1994) EMBO J. , vol.13 , pp. 6062-6075
    • Doye, V.1    Wepf, R.2    Hurt, E.C.3
  • 122
    • 0027978528 scopus 로고
    • Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif
    • Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C. Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 1994, 78:275-289.
    • (1994) Cell , vol.78 , pp. 275-289
    • Fabre, E.1    Boelens, W.C.2    Wimmer, C.3    Mattaj, I.W.4    Hurt, E.C.5
  • 123
    • 0029804030 scopus 로고    scopus 로고
    • ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae
    • Goldstein S.A., Price L.A., Rosenthal D.N., Pausch M.H. ORK1, a potassium-selective leak channel with two pore domains cloned from Drosophila melanogaster by expression in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:13256-13261.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13256-13261
    • Goldstein, S.A.1    Price, L.A.2    Rosenthal, D.N.3    Pausch, M.H.4
  • 124
    • 0029590122 scopus 로고
    • Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene
    • Heath C.V., Copeland C.S., Amberg D.C., Del Priore V., Snyder M., Cole C.N. Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene. J. Cell Biol. 1995, 131:1677-1697.
    • (1995) J. Cell Biol. , vol.131 , pp. 1677-1697
    • Heath, C.V.1    Copeland, C.S.2    Amberg, D.C.3    Del Priore, V.4    Snyder, M.5    Cole, C.N.6
  • 125
    • 0030911425 scopus 로고    scopus 로고
    • Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores
    • Segref A., Sharma K., Doye V., Hellwig A., Huber J., Luhrmann R., Hurt E. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 1997, 16:3256-3271.
    • (1997) EMBO J. , vol.16 , pp. 3256-3271
    • Segref, A.1    Sharma, K.2    Doye, V.3    Hellwig, A.4    Huber, J.5    Luhrmann, R.6    Hurt, E.7
  • 126
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C., Emig S., Segref A., Hurt E.C. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 1996, 84:265-275.
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 127
    • 84856117990 scopus 로고    scopus 로고
    • Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae
    • Hayakawa A., Babour A., Sengmanivong L., Dargemont C. Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae. J. Cell Biol. 2012, 196:19-27.
    • (2012) J. Cell Biol. , vol.196 , pp. 19-27
    • Hayakawa, A.1    Babour, A.2    Sengmanivong, L.3    Dargemont, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.